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Database: UniProt
Entry: A0A1L3JD62_9SPHN
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Original site: A0A1L3JD62_9SPHN 
ID   A0A1L3JD62_9SPHN        Unreviewed;       312 AA.
AC   A0A1L3JD62;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase {ECO:0000256|HAMAP-Rule:MF_01110};
DE            Short=AGPR {ECO:0000256|HAMAP-Rule:MF_01110};
DE            EC=1.2.1.38 {ECO:0000256|HAMAP-Rule:MF_01110};
DE   AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
DE            Short=NAGSA dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01110};
GN   Name=argC {ECO:0000256|HAMAP-Rule:MF_01110};
GN   ORFNames=LPB140_10210 {ECO:0000313|EMBL:APG63097.1};
OS   Sphingorhabdus lutea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1913578 {ECO:0000313|EMBL:APG63097.1, ECO:0000313|Proteomes:UP000242561};
RN   [1] {ECO:0000313|EMBL:APG63097.1, ECO:0000313|Proteomes:UP000242561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0140 {ECO:0000313|EMBL:APG63097.1,
RC   ECO:0000313|Proteomes:UP000242561};
RA   Kim E., Yi H.;
RT   "Sphingorhabdus sp. LPB0140, isolated from marine environment.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-
CC       glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
CC       {ECO:0000256|HAMAP-Rule:MF_01110}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate =
CC         H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:21588,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29123, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:57936, ChEBI:CHEBI:58349; EC=1.2.1.38;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01110};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 3/4. {ECO:0000256|HAMAP-
CC       Rule:MF_01110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110}.
CC   -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01110}.
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DR   EMBL; CP018154; APG63097.1; -; Genomic_DNA.
DR   RefSeq; WP_072559749.1; NZ_CP018154.1.
DR   AlphaFoldDB; A0A1L3JD62; -.
DR   STRING; 1913578.LPB140_10210; -.
DR   KEGG; sphl:LPB140_10210; -.
DR   OrthoDB; 9801289at2; -.
DR   UniPathway; UPA00068; UER00108.
DR   Proteomes; UP000242561; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   HAMAP; MF_01110; ArgC_type2; 1.
DR   InterPro; IPR023013; AGPR_AS.
DR   InterPro; IPR010136; AGPR_type-2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   NCBIfam; TIGR01851; argC_other; 1.
DR   PANTHER; PTHR32338:SF10; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR32338; N-ACETYL-GAMMA-GLUTAMYL-PHOSPHATE REDUCTASE, CHLOROPLASTIC-RELATED-RELATED; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS01224; ARGC; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01110};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_01110}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01110};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01110};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_01110}; Reference proteome {ECO:0000313|Proteomes:UP000242561}.
FT   DOMAIN          4..106
FT                   /note="Semialdehyde dehydrogenase NAD-binding"
FT                   /evidence="ECO:0000259|SMART:SM00859"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01110,
FT                   ECO:0000256|PROSITE-ProRule:PRU10010"
SQ   SEQUENCE   312 AA;  32968 MW;  79DB738CEB2C6307 CRC64;
     MSAKVFIDGA AGTTGIEIAE RLGERDDVQL IILSDDDRKN DDARRGAIIA ADVAILCLPD
     AAAKEAVAMA DAQNPTKFID ASTAHRIDPN WTYGFAEMRM GQQQAIENAQ FVSNPGCYPT
     GFLGLIAPLV DAGLLPKNLP YNVNAVSGYS GGGKELIAHF ESAGNIAFRG YALAHGHKHL
     PEMQLHAGLN HAPIFAPAVI NAYRGMVVEI MVPLGAFNIK STPQEMHDAL VSHYAGSKLV
     NVHEGDMPSE ILLLNGDDGN DGMTLYVAPS ADGAQLRLIA TLDNLGKGAS GAAVQNLNLM
     IGANIYEGLR LA
//
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